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- W2097616194 endingPage "a000919" @default.
- W2097616194 startingPage "a000919" @default.
- W2097616194 abstract "Even 30 years after its discovery, the tumor suppressor protein p53 is still somewhat of an enigma. p53's intimate and multifaceted role in the cell cycle is mirrored in its equally complex structural biology that is being unraveled only slowly. Here, we discuss key structural aspects of p53 function and its inactivation by oncogenic mutations. Concerted action of folded and intrinsically disordered domains of the highly dynamic p53 protein provides binding promiscuity and specificity, allowing p53 to process a myriad of cellular signals to maintain the integrity of the human genome. Importantly, progress in elucidating the structural biology of p53 and its partner proteins has opened various avenues for structure-guided rescue of p53 function in tumors. These emerging anticancer strategies include targeting mutant-specific lesions on the surface of destabilized cancer mutants with small molecules and selective inhibition of p53's degradative pathways." @default.
- W2097616194 created "2016-06-24" @default.
- W2097616194 creator A5068711489 @default.
- W2097616194 creator A5076882647 @default.
- W2097616194 date "2010-02-10" @default.
- W2097616194 modified "2023-10-12" @default.
- W2097616194 title "The Tumor Suppressor p53: From Structures to Drug Discovery" @default.
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